Interfacial properties of fractal and spherical whey protein aggregates

Mahmoudi, Najet; Axelos, Monique; Riaublanc, Alain

doi:10.1039/c1sm05262d

Cited by 50 publications

(33 citation statements)

References 59 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…After 7 days, this behavior progresses to large branched structures with a fractal morphology and a D f ~ 1.7 suggesting a DLA mechanism. This self‐organization behavior was previously detected in 33‐mer gliadin peptide and whey proteins . Peptide concentration could strongly influence the type of interactions established among monomers leading to differences in the self‐assembly behavior .…”

Section: Discussionsupporting

confidence: 69%

Structural conformation and self‐assembly process of p31‐43 gliadin peptide in aqueous solution. Implications for celiac disease

et al. 2019

View full text Add to dashboard Cite

Celiac disease (CeD) is a highly prevalent chronic immune-mediated enteropathy developed in genetically predisposed individuals after ingestion of a group of wheat proteins (called gliadins and glutenins). The 13mer agliadin peptide, p31-43, induces proinflammatory responses, observed by in vitro assays and animal models, that may contribute to innate immune mechanisms of CeD pathogenesis. Since a cellular receptor for p31-43 has not been identified, this raises the question of whether this peptide could mediate different biological effects. In this work, we aimed to characterize the p31-43 secondary structure by different biophysical and in silico techniques. By dynamic light scattering and using an oligomer/fibril-sensitive fluorescent probe, we showed the presence of oligomers of this peptide in solution. Furthermore, atomic force microscopy analysis showed p31-43 oligomers with different height distribution. Also, peptide concentration had a very strong influence on peptide self-organization process. Oligomers gradually increased their size at lower concentration. Whereas, at higher ones, oligomers increased their complexity, forming branched structures. By CD, we observed that p31-43 self-organized in a polyproline II conformation in equilibrium with b-sheets-like structures, whose pH remained stable in the range of 3-8. In addition, these findings were supported by molecular dynamics simulation. The formation of p31-43 nanostructures with increased b-sheet structure may help to explain the molecular etiopathogenesis in the induction of proinflammatory effects and subsequent damage at the intestinal mucosa in CeD.

show abstract

Section: Discussionsupporting

confidence: 69%

Structural conformation and self‐assembly process of p31‐43 gliadin peptide in aqueous solution. Implications for celiac disease

et al. 2019

View full text Add to dashboard Cite

show abstract

“…Surface hydrophobicity ( H 0 ) describes the ability of the protein to adsorb at the interface, and is closely correlated with the emulsifying properties (Mahmoudi et al ., ). The H 0 values of the six PPCs are shown in Table .…”

Section: Resultsmentioning

confidence: 97%

Characterisation of peanut protein concentrates from industrial aqueous extraction processing prepared by spray and freeze drying methods

Liu

Li²,

Jiang

et al. 2018

Int J of Food Sci Tech

View full text Add to dashboard Cite

Peanut protein concentrates (PPCs) were prepared by aqueous extraction processing (AEP), organic solvent extraction processing (SEP) and prepress-organic solvent extraction processing (P-SEP) and converted into powder by freeze and spray drying. The drying method showed an influence on the surface morphology and second structure of PPCs. Peanut protein concentrates of AEP were found to have lower protein contents, solubility and higher surface hydrophobicity, resulted in similar emulsion ability index (EAI) values and lower emulsion stability index (ESI) and water-holding capacity (WHC) values compared to PPCs of SEP and P-SEP. Foaming capacity was barely affected by oil extraction processing and drying methods, foaming stability was significantly influenced by oil extraction processing. Freeze-dried PPCs had higher solubility, WHC and fat absorption capacity than spray-dried PPCs, which was not the case for EAI and ESI. Hence, PPCs of AEP showed adequate functional properties, making AEP more appropriate for phytoprotein beverages.Oil extraction and drying methods J. Liu et al. 1598 Oil extraction and drying methods J. Liu et al.1599

show abstract

“…Depending on their intrinsic characteristics, especially the presence of covalent intramolecular bonds and their subsequent flexible or rigid structure, biopolymers adopt an extended or globular conformation at the interface. Biomolecule aggregates such as protein aggregates, often generated during food processes, can also adsorb at the interface and participate in emulsion stabilization (Euston and Hirst ; Chapleau and de Lamballerie‐Anton ; Relkin and others ; Mahmoudi and others ; Audebrand and others ).…”

Section: Prerequisites On O/w Emulsions and Interfacesmentioning

confidence: 99%

Lipid Oxidation in Oil‐in‐Water Emulsions: Involvement of the Interfacial Layer

Berton‐Carabin

Ropers

Génot

2014

Comp Rev Food Sci Food Safe

480

372

View full text Add to dashboard Cite

More polyunsaturated fats in processed foods and fewer additives are a huge demand of public health agencies and consumers. Consequently, although foods have an enhanced tendency to oxidize, the usage of antioxidants, especially synthetic antioxidants, is restrained. An alternate solution is to better control the localization of reactants inside the food matrix to limit oxidation. This review establishes the state-of-the-art on lipid oxidation in oil-in-water (O/W) emulsions, with an emphasis on the role of the interfacial region, a critical area in the system in that respect. We first provide a summary on the essential basic knowledge regarding (i) the structure of O/W emulsions and interfaces and (ii) the general mechanisms of lipid oxidation. Then, we discuss the factors involved in the development of lipid oxidation in O/W emulsions with a special focus on the role played by the interfacial region. The multiple effects that can be attributed to emulsifiers according to their chemical structure and their location, and the interrelationships between the parameters that define the physicochemistry and structure of emulsions are highlighted. This work sheds new light on the interpretation of reported results that are sometimes ambiguous or contradictory.

show abstract

Interfacial properties of fractal and spherical whey protein aggregates

Cited by 50 publications

References 59 publications

Structural conformation and self‐assembly process of p31‐43 gliadin peptide in aqueous solution. Implications for celiac disease

Structural conformation and self‐assembly process of p31‐43 gliadin peptide in aqueous solution. Implications for celiac disease

Characterisation of peanut protein concentrates from industrial aqueous extraction processing prepared by spray and freeze drying methods

Lipid Oxidation in Oil‐in‐Water Emulsions: Involvement of the Interfacial Layer

Contact Info

Product

Resources

About